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Q9UBS8 (RNF14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RNF14

EC=6.3.2.-
Alternative name(s):
Androgen receptor-associated protein 54
HFB30
RING finger protein 14
Triad2 protein
Gene names
Name:RNF14
Synonyms:ARA54
ORF Names:HRIHFB2038
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription. Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with the ubiquitin-conjugating enzymes UBE2E1 and UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-regulated it promotes AR transcriptional activity. Ref.11

Subcellular location

Cytoplasm. Nucleus Ref.8.

Tissue specificity

Widely expressed.

Domain

The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway By similarity.

The RING-type zinc finger is essential for the interaction with UBE2E2.

Post-translational modification

RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination.

Sequence similarities

Belongs to the RBR family. RNF14 subfamily.

Contains 1 IBR-type zinc finger.

Contains 2 RING-type zinc fingers.

Contains 1 RWD domain.

Caution

Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement Ref.9PubMed 15572661. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

protein ubiquitination

Inferred from expression pattern Ref.9. Source: UniProtKB

regulation of androgen receptor signaling pathway

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

response to estradiol

Inferred from direct assay PubMed 15831516. Source: BHF-UCL

signal transduction

Traceable author statement Ref.2. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionandrogen receptor binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2. Source: UniProtKB

small conjugating protein ligase activity

Inferred from direct assay Ref.9. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP102752EBI-2130308,EBI-608057

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBS8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UBS8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474E3 ubiquitin-protein ligase RNF14
PRO_0000056057

Regions

Domain11 – 137127RWD
Zinc finger220 – 27051RING-type 1; atypical
Zinc finger289 – 35062IBR-type
Zinc finger404 – 43330RING-type 2; degenerate
Region361 – 474114Interaction with androgen receptor
Coiled coil351 – 39545 Potential
Motif37 – 459D-box

Amino acid modifications

Modified residue3481Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 126126Missing in isoform 2.
VSP_045780

Experimental info

Mutagenesis2201C → S: Loss of interaction with UBE2E2 and of autoubiquitination. Ref.9
Sequence conflict321Q → R in CAG32983. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 529E3F5AF38A5DAD

FASTA47453,837
        10         20         30         40         50         60 
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQN 

        70         80         90        100        110        120 
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS 

       130        140        150        160        170        180 
VVLFAWMQFL KEETLAYLNI VSPFELKIGS QKKVQRRTAQ ASPNTELDFG GAAGSDVDQE 

       190        200        210        220        230        240 
EIVDERAVQD VESLSNLIQE ILDFDQAQQI KCFNSKLFLC SICFCEKLGS ECMYFLECRH 

       250        260        270        280        290        300 
VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSSL 

       310        320        330        340        350        360 
DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL 

       370        380        390        400        410        420 
RNEYLQADEA NKRLLDQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM 

       430        440        450        460        470 
TCTGCMQYFC WICMGSLSRA NPYKHFNDPG SPCFNRLFYA VDVDDDIWED EVED 

« Hide

Isoform 2 [UniParc].

Checksum: C43770874596DD0C
Show »

FASTA34839,634

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel human gene (HFB30) which encodes a protein with a RING finger motif."
Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.-A.
Biochim. Biophys. Acta 1445:232-236(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[2]"Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor."
Kang H.-Y., Yeh S., Fujimoto N., Chang C.
J. Biol. Chem. 274:8570-8576(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
Tissue: Prostate.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Thyroid.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Selection system for genes encoding nuclear-targeted proteins."
Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-474 (ISOFORM 1), SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[9]"N-terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8."
Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.
Eur. J. Biochem. 268:2725-2732(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-220.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination."
Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D., Qiu Y.
Cancer Cell 15:270-282(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AR.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022663 mRNA. Translation: BAA78677.1.
AF060544 mRNA. Translation: AAD21842.1.
AK023884 mRNA. Translation: BAG51234.1.
AK057868 mRNA. No translation available.
CR456702 mRNA. Translation: CAG32983.1.
AC005740 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61895.1.
CH471062 Genomic DNA. Translation: EAW61896.1.
CH471062 Genomic DNA. Translation: EAW61897.1.
BC126185 mRNA. Translation: AAI26186.1.
BC144061 mRNA. Translation: AAI44062.1.
AB015333 mRNA. Translation: BAA34792.1.
CCDSCCDS4270.1. [Q9UBS8-1]
CCDS4271.1. [Q9UBS8-2]
RefSeqNP_001188294.1. NM_001201365.1. [Q9UBS8-1]
NP_004281.1. NM_004290.4. [Q9UBS8-1]
NP_899645.1. NM_183398.2. [Q9UBS8-2]
NP_899646.1. NM_183399.2. [Q9UBS8-1]
NP_899647.1. NM_183400.2. [Q9UBS8-1]
NP_899648.1. NM_183401.2. [Q9UBS8-1]
XP_005268593.1. XM_005268536.1. [Q9UBS8-1]
XP_005268594.1. XM_005268537.1. [Q9UBS8-1]
XP_005268595.1. XM_005268538.1. [Q9UBS8-1]
XP_005268596.1. XM_005268539.1. [Q9UBS8-2]
XP_005268597.1. XM_005268540.1. [Q9UBS8-2]
XP_005268598.1. XM_005268541.1. [Q9UBS8-2]
UniGeneHs.483616.

3D structure databases

ProteinModelPortalQ9UBS8.
SMRQ9UBS8. Positions 188-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114968. 21 interactions.
IntActQ9UBS8. 16 interactions.
MINTMINT-1187964.
STRING9606.ENSP00000324956.

PTM databases

PhosphoSiteQ9UBS8.

Polymorphism databases

DMDM17380293.

Proteomic databases

MaxQBQ9UBS8.
PaxDbQ9UBS8.
PRIDEQ9UBS8.

Protocols and materials databases

DNASU9604.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347642; ENSP00000324956; ENSG00000013561. [Q9UBS8-1]
ENST00000356143; ENSP00000348462; ENSG00000013561. [Q9UBS8-1]
ENST00000394514; ENSP00000378022; ENSG00000013561. [Q9UBS8-2]
ENST00000394519; ENSP00000378027; ENSG00000013561. [Q9UBS8-1]
ENST00000394520; ENSP00000378028; ENSG00000013561. [Q9UBS8-1]
GeneID9604.
KEGGhsa:9604.
UCSCuc003lly.3. human. [Q9UBS8-1]

Organism-specific databases

CTD9604.
GeneCardsGC05P141358.
HGNCHGNC:10058. RNF14.
HPAHPA008716.
MIM605675. gene.
neXtProtNX_Q9UBS8.
PharmGKBPA34423.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266709.
HOVERGENHBG057296.
InParanoidQ9UBS8.
KOK11971.
OMAQYFCWLC.
PhylomeDBQ9UBS8.
TreeFamTF314401.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UBS8.
BgeeQ9UBS8.
CleanExHS_RNF14.
GenevestigatorQ9UBS8.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR002867. Znf_C6HC.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF01485. IBR. 2 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTSM00647. IBR. 2 hits.
SM00184. RING. 1 hit.
SM00591. RWD. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50908. RWD. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF14. human.
GeneWikiRNF14.
GenomeRNAi9604.
NextBio36027.
PROQ9UBS8.
SOURCESearch...

Entry information

Entry nameRNF14_HUMAN
AccessionPrimary (citable) accession number: Q9UBS8
Secondary accession number(s): A0AV26 expand/collapse secondary AC list , A6NMR2, A8MTW5, B3KN72, B7ZLV2, D3DQE4, O94793, Q6IBV0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM